Molecular and Cellular Biochemistry

, Volume 269, Issue 1, pp 203–207 | Cite as

Opposing effects of two osmolytes – trehalose and glycerol – on thermal inactivation of rabbit muscle 6-phosphofructo-1-kinase

  • Joana Faber-Barata
  • Mauro Sola-Penna


Trehalose and glycerol are known as good stabilizers of function and structure of several macromolecules against stress conditions. We previously reported that they have comparable effectiveness on protecting two yeast cytosolic enzymes against thermal inactivation. However, enzyme protection has always been associated to a decrease in catalytic activity at the stabilizing conditions i.e., the presence of the protective molecule. In the present study we tested trehalose and glycerol on thermal protection of the mammalian cytosolic enzyme phosphofructokinase. Here we found that trehalose was able to protect phosphofructokinase against thermal inactivation as well as to promote an activation of its catalytic activity. The enzyme incubated in the presence of 1 M trehalose did not present any significant inactivation within 2 h of incubation at 50 C, contrasting to control experiments where the enzyme was fully inactivated during the same period exhibiting a t0.5 for thermal inactivation of 56± 5 min. On the other hand, enzyme incubated in the presence of 37.5% (v/v) glycerol was not protected against incubation at 50 C. Indeed, when phosphofructokinase was incubated for 45 min at 50 C in the presence of lower concentrations of glycerol (7.5–25%, v/v), the remaining activity was 2–4 times lower than control. These data show that the compatibility of effects previously shown for trehalose and glycerol with some yeast cytosolic enzymes can not be extended to all globular enzyme system. In the case of phosphofructokinase, we believe that its property of shifting between several different complex oligomers configurations can be influenced by the physicochemical properties of the stabilizing molecules. (Mol Cell Biochem 269: 203)


counteracting effects osmolytes PFK protein stabilization tetramers 


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Copyright information

© Springer Science + Business Media, Inc. 2005

Authors and Affiliations

  1. 1.Laboratório de Enzimologia e Controle do Metabolismo (LabECoM), Departamento de Fármacos, Faculdade de FarmáciaUniversidade Federal do Rio de JaneiroRio de JaneiroBrasil
  2. 2.Departamento de Bioquímica Médica, Instituto de Ciências BiomédicasUniversidade Federal do Rio de JaneiroRio de JaneiroBrasil

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